ID K6U6I5_9CLOT Unreviewed; 644 AA.
AC K6U6I5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=ABC-type multidrug transport system, ATPase and permease component {ECO:0000313|EMBL:EKQ57506.1};
GN ORFNames=A370_00881 {ECO:0000313|EMBL:EKQ57506.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ57506.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ57506.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ57506.1}.
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DR EMBL; ALXI01000021; EKQ57506.1; -; Genomic_DNA.
DR AlphaFoldDB; K6U6I5; -.
DR STRING; 1196322.A370_00881; -.
DR PATRIC; fig|1196322.3.peg.859; -.
DR eggNOG; COG1132; Bacteria.
DR Proteomes; UP000001325; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18547; ABC_6TM_Tm288_like; 1.
DR CDD; cd03254; ABCC_Glucan_exporter_like; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR PANTHER; PTHR24221:SF499; FATTY ACID ABC TRANSPORTER ATP-BINDING_PERMEASE PROTEIN; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001325};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 43..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..339
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 405..639
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 644 AA; 71365 MW; 07DF3DCE0A9911F8 CRC64;
MSQNNAKAPR AMRGPGGPRG HAKVSKDSLK TLKRLLAYVL KEYKVLFIIV LVTIIISSLA
NVIGTLFLRN LIDDYIAPLL KASGAPDFGP LLKMIITLAT IYLVGVLATY IYSRIMIIIS
QGSLKKIRDD MFAHMETLPI KFFDTHAHGD VMSLYTNDTD ALRQMISQGI PQLLSAIITV
VSVFISMIFL SIPLTIVQIV IIFLMVNVTK FIGAKSGKYF GAQQRDLGAV NGYIEEMMEG
QKVVKVFCHE EEARINFDKL NDALCNSANN ANKYANALMP VVNNIGYINY VTVAIFGSVI
AIGEFAGFTI GALASFLQLT RTFSQTVNQM AQQFNFVIMA LAGAERIFKL LDEEKETDEG
YVTLVNAIED ENRKLTEAKK RTGIWAWKHP HEDGTTTYTK LLGEVVFDDV DFGYNDEKII
LHNIKLFAKP GQKIAFVGAT GAGKTTITNL INRFYDIQDG KIRYDGININ KIKKDDLRSS
LGIVLQDAHL FTGTVSDNIR YGKLDATDEE VRAAAKLANA DTFIRHLPKG YDTVLTGDGG
SLSQGQRQLL TIARAAIADP PVLILDEATS SIDTRTEKIV QDGMDKLMKG RTVFVIAHRL
STIKNSDVIM VLDQGKIIER GNHDDLIEQR GKYYQLYTGA FELS
//
